ArticleBiotechnology progress
A novel endo-β-N-acetylglucosaminidase releases specific N-glycans depending on different reaction conditions.
Article in Biotechnology progress. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 24 citations in OpenAlex.
- Substrate Versatility of a Recombinant Bifidobacterial Endoglycosidase:International journal of molecular sciences · 2026Article
- Fucosidosis: A Review of a Rare Disease.International journal of molecular sciences · 2025Review
- Identification and comparison ofFood chemistry: X · 2025Article
- Human Milk Oligosaccharides: Decoding Their Structural Variability, Health Benefits, and the Evolution of Infant Nutrition.Nutrients · 2024Review
- Food glycomics: Dealing with unexpected degradation of oligosaccharides during sample preparation and analysis.Journal of food and drug analysis · 2022Article
- Role of milk glycome in prevention, treatment, and recovery of COVID-19.Frontiers in nutrition · 2022Review
- Immobilization of a Bifidobacterial Endo-Frontiers in bioengineering and biotechnology · 2022Article
- Potential applications of recombinant bifidobacterial proteins in the food industry, biomedicine, process innovation and glycobiology.Food science and biotechnology · 2021Review
- Microbial Glycoside Hydrolases in the First Year of Life: An Analysis Review on Their Presence and Importance in Infant Gut.Frontiers in microbiology · 2021Review
- Potential Applications of Endo-β-Frontiers in nutrition · 2021Review
- Article
- Structural insights of two novel N-acetyl-glucosaminidase enzymes through in silico methods.Turkish journal of chemistry · 2020Article
- Molecular Insights IntoFrontiers in microbiology · 2020Review
- Immobilization of an Endo-β-Catalysts (Basel, Switzerland) · 2018Article
- Recent advances in immobilization strategies for glycosidases.Biotechnology progress · 2017Review
- Characterization of recombinant human lactoferrin N-glycans expressed in the milk of transgenic cows.PloS one · 2017Article
- Oligosaccharides Released from Milk Glycoproteins Are Selective Growth Substrates for Infant-Associated Bifidobacteria.Applied and environmental microbiology · 2016Article
- Characterizing the release of bioactive N-glycans from dairy products by a novel endo-β-N-acetylglucosaminidase.Biotechnology progressArticle
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Milk glycoproteins are involved in different functions and contribute to different cellular processes, including adhesion and signaling, and shape the development of the infant microbiome. Methods have been developed to study the complexities of milk protein glycosylation and understand the role of N-glycans in protein functionality. Endo-β-N-acetylglucosaminidase (EndoBI-1) isolated from Bifidobacterium longum subsp. infantis ATCC 15697 is a recently isolated heat-stable enzyme that cleaves the N-N'-diacetyl chitobiose moiety found in the N-glycan core. The effects of different processing conditions (pH, temperature, reaction time, and enzyme/protein ratio) were evaluated for their ability to change EndoBI-1 activity on bovine colostrum whey glycoproteins using advanced mass spectrometry. This study shows that EndoBI-1 is able to cleave a high diversity of N-glycan structures. Nano-LC-Chip-Q-TOF MS data also revealed that different reaction conditions resulted in different N-glycan compositions released, thus modifying the relative abundance of N-glycan types. In general, more sialylated N-glycans were released at lower temperatures and pH values. These results demonstrated that EndoBI-1 is able to release a wide variety of N-glycans, whose compositions can be selectively manipulated using different processing conditions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.